3vw5: Difference between revisions
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==Crystal structure of sugar epimerase from ruminal bacterium== | ==Crystal structure of sugar epimerase from ruminal bacterium== | ||
<StructureSection load='3vw5' size='340' side='right' caption='[[3vw5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3vw5' size='340' side='right' caption='[[3vw5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vw5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3vw5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27210 Atcc 27210]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VW5 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1264 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1264 ATCC 27210])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellobiose_epimerase Cellobiose epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.11 5.1.3.11] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellobiose_epimerase Cellobiose epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.11 5.1.3.11] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vw5 RCSB], [http://www.ebi.ac.uk/pdbsum/3vw5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw5 OCA], [http://pdbe.org/3vw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vw5 RCSB], [http://www.ebi.ac.uk/pdbsum/3vw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vw5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CEEP_RUMA7 CEEP_RUMA7]] Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man).[HAMAP-Rule:MF_00929] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3vw5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 27210]] | |||
[[Category: Cellobiose epimerase]] | [[Category: Cellobiose epimerase]] | ||
[[Category: Fujiwara, T]] | [[Category: Fujiwara, T]] | ||
[[Category: Saburi, W]] | [[Category: Saburi, W]] | ||
Revision as of 01:24, 5 August 2016
Crystal structure of sugar epimerase from ruminal bacteriumCrystal structure of sugar epimerase from ruminal bacterium
Structural highlights
Function[CEEP_RUMA7] Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man).[HAMAP-Rule:MF_00929] Publication Abstract from PubMedEnzymatic epimerization is an important modification for carbohydrates to acquire diverse functions attributable to their stereoisomers. Cellobiose 2-epimerase (CE) catalyzes interconversion between d-glucose and d-mannose residues at the reducing end of beta-1,4-linked oligosaccharides. Here, we solved the structure of Ruminococcus albus CE (RaCE). The structure of RaCE showed strong similarity to those of N-acetyl-D-glucosamine 2-epimerase and aldose-ketose isomerase YihS with a high degree of conservation of residues around the catalytic center, although sequence identity between them is low. Based on structural comparison, we found that His184 is required for RaCE activity as the third histidine added to two essential histidines in other sugar epimerases/isomerases. This finding was confirmed by mutagenesis, suggesting a new catalytic mechanism for CE involving three histidines. Crystal structure of Ruminococcus albus cellobiose 2-epimerase: structural insights into epimerization of unmodified sugar.,Fujiwara T, Saburi W, Inoue S, Mori H, Matsui H, Tanaka I, Yao M FEBS Lett. 2013 Apr 2;587(7):840-6. doi: 10.1016/j.febslet.2013.02.007. Epub 2013, Feb 24. PMID:23462136[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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